SpermatogenesisOnline 1.0
 

Tag Content
SG ID
SG00001912 
UniProt Accession
Theoretical PI
8.27  
Molecular Weight
23794 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Timp1 
Gene Synonyms/Alias
Timp-1 
Protein Name
Metalloproteinase inhibitor 1 
Protein Synonyms/Alias
Tissue inhibitor of metalloproteinases 1;TIMP-1Flags: Precursor 
Organism
Rattus norvegicus (Rat) 
NCBI Taxonomy ID
10116 
Chromosome Location
chr:X;12542496-12547094;-1
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Description
Temporarily unavailable 
The information of related literatures
1. L. M. Gronning, J. E. Wang, A. H. Ree, T. B. Haugen, K. Tasken and K. A. Tasken (2000) Regulation of tissue inhibitor of metalloproteinases-1 in rat Sertoli cells. Biol Reprod 62(4): 1040-6. 

Abstract
In the testis, FSH has been shown to induce the expression and secretion of tissue inhibitor of metalloproteinases-1 (TIMP-1) from Sertoli cells in vitro. This study was performed to elucidate further the cellular origin of testicular TIMP-1 and its expression by hormonal and paracrine factors. This is the first report on the expression of testicular TIMP-1 in vivo. TIMP-1 mRNA in whole testis was decreased after hypophysectomy and strongly increased by the injection of FSH-S17 to hypophysectomized rats. Primary cultures of both peritubular and Sertoli cells showed basal expression of TIMP-1 mRNA. In contrast, we were unable to detect TIMP-1 mRNA in Leydig cells, freshly isolated immature germ cells (primary spermatocytes and spermatids), or residual bodies. We further show that treatment of Sertoli cells with 8-(4-chlorophenyl)thio-cAMP (8-CPTcAMP) in combination with 12-O-tetradecanoylphorbol 13-acetate (TPA) or Ca(2+) inducers (calcium ionophore A23187 or thapsigargin) had additive (TPA) and synergistic effects (Ca(2+)) on the level of TIMP-1 mRNA and secreted protein. We also show that both the level of TIMP-1 mRNA and secreted protein from Sertoli cells were strongly increased by residual bodies, as well as by the cytokine interleukin-1alpha. TIMP-1 was not up-regulated by either 8-CPTcAMP or interleukin-1alpha in peritubular cells. In contrast to the regulated secretory fraction of TIMP-1, we also detected constitutively expressed immunoreactive TIMP-1 in the nucleus of Sertoli cells, suggesting a role of nuclear TIMP-1 in these cells. In conclusion, our data show that secretion of TIMP-1 from Sertoli cells is highly regulated by hormonal and local processes in the testis, indicating that TIMP-1 is of physiological importance during both testicular development and spermatogenesis. PMID: [10727275] 

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Figures for illustrating the function of this protein/gene
Function
Complexes with metalloproteinases (such as collagenases)and irreversibly inactivates them by binding to their catalyticzinc cofactor. Also stimulates steroidogenesis by Leydig andovarian granuloma cells; procathepsin L is required for maximalactivity. 
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Subcellular Location
Secreted. 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0005604 C:basement membrane IEA:Compara.
GO:0031012 C:extracellular matrix IDA:RGD.
GO:0046872 F:metal ion binding IEA:UniProtKB-KW.
GO:0008191 F:metalloendopeptidase inhibitor activity TAS:RGD.
GO:0007568 P:aging IEP:RGD.
GO:0001775 P:cell activation IMP:RGD.
GO:0043249 P:erythrocyte maturation IEA:UniProtKB-KW.
GO:0043066 P:negative regulation of apoptotic process IMP:RGD.
GO:0051045 P:negative regulation of membrane protein ectodomain proteolysis IEA:Compara.
GO:0034097 P:response to cytokine stimulus IEP:RGD.
GO:0043434 P:response to peptide hormone stimulus IEP:RGD.
GO:0006694 P:steroid biosynthetic process IEA:UniProtKB-KW.
GO:0042060 P:wound healing IEP:RGD.
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Interpro
IPR001134;    Netrin_domain.
IPR001820;    Prot_inh_TIMP.
IPR008993;    TIMP-like_OB-fold.
IPR015611;    TIMP1.
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Pfam
PF00965;    TIMP;    1.
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SMART
SM00206;    NTR;    1.
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PROSITE
PS50189;    NTR;    1.
PS00288;    TIMP;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
Experiment identified 
Protein sequence Annotation
SIGNAL        1     23
CHAIN        24    217       Metalloproteinase inhibitor 1.
                             /FTId=PRO_0000034329.
DOMAIN       24    147       NTR.
REGION       24     28       Involved in metalloproteinase-binding (By
                             similarity).
REGION       90     91       Involved in metalloproteinase-binding (By
                             similarity).
METAL        24     24       Zinc; via amino nitrogen and carbonyl
                             oxygen; shared with metalloproteinase
                             partner (By similarity).
CARBOHYD     77     77       N-linked (GlcNAc...) (Potential).
CARBOHYD    101    101       N-linked (GlcNAc...) (Potential).
DISULFID     24     93       By similarity.
DISULFID     26    122       By similarity.
DISULFID     36    147       By similarity.
DISULFID    150    197       By similarity.
DISULFID    155    160       By similarity.
DISULFID    168    189       By similarity.
CONFLICT     80     81       GF -> DI (in Ref. 5; AAB08483).
CONFLICT     88     88       A -> V (in Ref. 6; AAA51653).
CONFLICT    103    103       S -> R (in Ref. 5; AAB08483).
CONFLICT    129    130       HN -> AS (in Ref. 5; AAB08483).
CONFLICT    136    140       QKAFV -> RKGLT (in Ref. 5; AAB08483).
CONFLICT    149    149       V -> L (in Ref. 6; AAA51653).
CONFLICT    157    157       A -> V (in Ref. 5; AAB08483).
CONFLICT    166    166       S -> T (in Ref. 5; AAB08483).
CONFLICT    185    187       DHF -> RHL (in Ref. 5; AAB08483).
CONFLICT    195    195       D -> G (in Ref. 5; AAB08483).
CONFLICT    201    201       Y -> S (in Ref. 5; AAB08483).
CONFLICT    204    205       VS -> SR (in Ref. 5; AAB08483).
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Nucleotide Sequence
Length: 737 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 217 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
 Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
View Microarray data
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